ArticleThe Journal of cell biology1997
Expression of matrix metalloproteinases during rat skin wound healing: evidence that membrane type-1 matrix metalloproteinase is a stromal activator of pro-gelatinase A.
Article in The Journal of cell biology, 1997. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 45 papers, 1 of them a synthesis that pooled it.
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Who cites it
45 citing papers in PubMed, 1 synthesis or guideline pooled it, 223 citations in OpenAlex.
- What Is the Impact of Depletion of Immunoregulatory Genes on Wound Healing? A Systematic Review of Preclinical Evidence.Oxidative medicine and cellular longevity · 2020Pooled it
- Inhibition of Metalloproteinases-2, -9, and -14 Suppresses Papillary Thyroid Carcinoma Cell Migration and Invasion.International journal of molecular sciences · 2025Article
- Defect of Interferon γ Leads to Impaired Wound Healing through Prolonged Neutrophilic Inflammatory Response and Enhanced MMP-2 Activation.International journal of molecular sciences · 2019Article
- TRIM58/cg26157385 methylation is associated with eight prognostic genes in lung squamous cell carcinoma.Oncology reports · 2018Article
- DDR1 and DDR2 in skin.Cell adhesion & migration · 2018Review
- Skin and Its Regenerative Powers: An Alliance between Stem Cells and Their Niche.Developmental cell · 2017Review
- Discoidin domain receptor 2 mediates collagen-induced activation of membrane-type 1 matrix metalloproteinase in human fibroblasts.The Journal of biological chemistry · 2017Article
- Defining stem cell dynamics and migration during wound healing in mouse skin epidermis.Nature communications · 2017Article
- Stromal fibroblasts facilitate cancer cell invasion by a novel invadopodia-independent matrix degradation process.Oncogene · 2016Article
- Matrix Metalloproteinase 10 Degradomics in Keratinocytes and Epidermal Tissue Identifies Bioactive Substrates With Pleiotropic Functions.Molecular & cellular proteomics : MCP · 2015Article
- Understanding the host response to cell-laden poly(ethylene glycol)-based hydrogels.Biomaterials · 2013Article
- A comparison of epithelial-to-mesenchymal transition and re-epithelialization.Seminars in cancer biology · 2012Review
- Pressure overload-dependent membrane type 1-matrix metalloproteinase induction: relationship to LV remodeling and fibrosis.American journal of physiology. Heart and circulatory physiology · 2012Article
- Impaired dermal wound healing in discoidin domain receptor 2-deficient mice associated with defective extracellular matrix remodeling.Fibrogenesis & tissue repair · 2011Article
- Variability in melanoma metalloproteinase expression profiling.Journal of biomolecular techniques : JBT · 2010Article
- Cardiac restricted overexpression of membrane type-1 matrix metalloproteinase causes adverse myocardial remodeling following myocardial infarction.The Journal of biological chemistry · 2010Article
- Metalloproteinase binding proteins: WO2009097397.Expert opinion on therapeutic patents · 2010Article
- 17beta-estradiol inhibits wound healing in male mice via estrogen receptor-alpha.The American journal of pathology · 2010Article
- Extracellular matrix, inflammation, and the angiogenic response.Cardiovascular research · 2010Review
- Role of matrix metalloproteinases in epithelial migration.Journal of cellular biochemistry · 2009Review
Corrections and comments
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Authors and funding
6 authors at 2 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Skin wound healing depends on cell migration and extracellular matrix remodeling. Both processes, which are necessary for reepithelization and restoration of the underlying connective tissue, are believed to involve the action of extracellular proteinases. We screened cDNA libraries and we found that six matrix metalloproteinase genes were highly expressed during rat skin wound healing. They were namely those of stromelysin 1, stromelysin 3, collagenase 3, gelatinase A (GelA), gelatinase B, and membrane type-1 matrix metalloproteinase (MT1-MMP). The expression kinetics of these MMP genes, the tissue distribution of their transcripts, the results of cotransfection experiments in COS-1 cells, and zymographic analyses performed using microdissected rat wound tissues support the possibility that during cutaneous wound healing pro-GelA and pro-gelatinase B are activated by MT1-MMP and stromelysin 1, respectively. Since MT1-MMP has been demonstrated to be a membrane-associated protein (Sato, H., T. Takino, Y. Okada, J. Cao, A. Shinagawa, E. Yamamoto, and M. Seiki. 1994. Nature (Lond.). 370: 61-65), our finding that GelA and MT1-MMP transcripts were expressed in stromal cells exhibiting a similar tissue distribution suggests that MT1-MMP activates pro-GelA at the stromal cell surface. This possibility is further supported by our observation that the processing of pro-GelA to its mature form correlated to the detection of MT1-MMP in cell membranes of rat fibroblasts expressing the MT1-MMP and GelA genes. These observations, together with the detection of high levels of the mature GelA form in the granulation tissue but not in the regenerating epidermis, suggest that MT1-MMP and GelA contribute to the restoration of connective tissue during rat skin wound healing.
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